Short Communication - International Research Journal of Biochemistry and Bioinformatics ( 2021) Volume 11, Issue 3
Time-resolved diffraction experiments at an X-ray free electron laser reveals structural changes in bacteriorhodopsin - Richard Neutze - Public university in Gothenburg, Sweden
Richard Neutze*,
Eriko Nango,
Tomoyuki Tanaka,
Takanori Nakane,
So Iwata,
Antoine Royant,
Jorg Standfuss,
Przemyslaw Nogly and
Cecilia Wickstrand
Public university in Gothenburg, Sweden
*Corresponding Author:
Richard Neutze, Public university in Gothenburg,
Sweden,
Published:
28-Jun-2021
Abstract
X-ray free electron lasers (XFEL) provide a billionfold jump in the peak X-ray brilliance when
compared with synchrotron radiation. One area
where XFEL radiation has an impact is time-resolved
structural studies of protein conformational changes.
This presentation will describe how we used time
resolved serial femtosecond crystallography at an
XFEL to probe light-driven structural changes in
bacteriorhodopsin.
Bacteriorhodopsin is a light-driven proton pump which has long been used as a model system in biophysics. The mechanism by which light-driven isomerization of a retinal chromophore is coupled to the transport of protons †œup-hill†• against a transmembrane proton concentration gradient involves protein structural changes.
Collaborative studies performed at SACLA (the Japanese XFEL) have probed structural changes in microcrystals on a time-scale from nanoseconds to milliseconds.
Structural results from these studies enabled a complete picture of structural changes occurring during proton pumping by bacteriorhodopsin to be recovered
